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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4896
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pubmed:dateCreated |
1989-4-14
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pubmed:abstractText |
An analysis of the aminoacylation kinetics of unmodified yeast tRNAPhe mutants revealed that five single-stranded nucleotides are important for its recognition by yeast phenylalanyl-tRNA synthetase, provided they were positioned correctly in a properly folded tRNA structure. When four other tRNAs were changed to have these five nucleotides, they became near-normal substrates for the enzyme.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
243
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1363-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2646717-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:2646717-Base Sequence,
pubmed-meshheading:2646717-Escherichia coli,
pubmed-meshheading:2646717-Models, Molecular,
pubmed-meshheading:2646717-Molecular Sequence Data,
pubmed-meshheading:2646717-Mutation,
pubmed-meshheading:2646717-Nucleic Acid Conformation,
pubmed-meshheading:2646717-Phenylalanine-tRNA Ligase,
pubmed-meshheading:2646717-Plants,
pubmed-meshheading:2646717-RNA, Transfer, Amino Acid-Specific,
pubmed-meshheading:2646717-RNA, Transfer, Phe,
pubmed-meshheading:2646717-Schizosaccharomyces,
pubmed-meshheading:2646717-Transcription, Genetic,
pubmed-meshheading:2646717-Triticum
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pubmed:year |
1989
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pubmed:articleTitle |
Nucleotides in yeast tRNAPhe required for the specific recognition by its cognate synthetase.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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